|
Ferritin
Ferritin is a universal intracellular and extracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including archaea, bacteria, algae, higher plants, and animals. It is the primary ''intracellular iron-storage protein'' in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form. In humans, it acts as a buffer against iron deficiency and iron overload. Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum where it functions as an iron carrier. Plasma ferritin is also an indirect marker of the total amount of iron stored in the body; hence, serum ferritin is used as a diagnostic test for iron-deficiency anemia and iron overload. Aggregated ferritin transforms into a water insoluble, crystalline and amorphous form of storage iron called hemosiderin. Ferritin is a globular protein complex consisting of 24 protein subuni ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ferritin Light Chain
Ferritin light chain is a protein that in humans is encoded by the ''FTL'' gene. Ferritin is the major protein responsible for storing intracellular iron in prokaryotes and eukaryotes. It is a heteropolymer consisting of 24 subunits, heavy and light ferritin chains. This gene has multiple pseudogenes. It is abnormally expressed in fetuses of both in vitro fertilization, IVF and intracytoplasmic sperm injection, ICSI, which may contribute to the increase risk of birth defects in these assisted reproductive technology, assisted reproductive technologies. Function Iron is extremely important in the development of neurons, transport through iron-sulfur clusters, the electron transport chain, and synthesis and breakdown of neurotransmitters. The function of the FTL is to act as both an iron reservoir and to remove excess iron from the body. Since iron plays a role in electron transfer, there is potential for the generation of free, highly toxic radicals which makes the role of the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FTH1
Ferritin heavy chain is a ferroxidase enzyme that in humans is encoded by the ''FTH1'' gene. FTH1 gene is located on chromosome 11, and its mutation causes Hemochromatosis type 5. Function This gene encodes the heavy subunit of ferritin, the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in ferritin proteins are associated with several neurodegenerative diseases. This gene has multiple pseudogenes. Several alternatively spliced transcript variants have been observed, but their biological validity has not been determined. Interactions FTH1 has been shown to interact with ferritin light chain. See also * Ferritin Ferritin is a universal intracellular and extracellular ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iron Overload
Iron overload is the abnormal and increased accumulation of total iron in the body, leading to organ damage. The primary mechanism of organ damage is oxidative stress, as elevated intracellular iron levels increase free radical formation via the Fenton reaction. Iron overload is often ''primary'' (i.e hereditary haemochromatosis, aceruloplasminemia) but may also be ''secondary'' to other causes (i.e. transfusional iron overload). Iron deposition most commonly occurs in the liver, pancreas, skin, heart, and joints. People with iron overload classically present with the triad of liver cirrhosis, secondary diabetes mellitus, and bronze skin. However, due to earlier detection nowadays, symptoms are often limited to general chronic malaise, arthralgia, and hepatomegaly. Signs and symptoms Organs most commonly affected by hemochromatosis include the liver, heart, and endocrine glands. Hemochromatosis may present with the following clinical syndromes: * liver: chronic liver di ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iron-deficiency Anemia
Iron-deficiency anemia is anemia caused by a iron deficiency, lack of iron. Anemia is defined as a decrease in the number of red blood cells or the amount of hemoglobin in the blood. When onset is slow, symptoms are often vague such as Fatigue (medical), feeling tired, weak, dyspnea, short of breath, or having decreased ability to exercise. Anemia that comes on quickly often has more severe symptoms, including decreased level of consciousness, confusion, Presyncope, feeling like one is going to pass out or increased thirst. Anemia is typically significant before a person becomes noticeably pallor, pale. Children with iron deficiency anemia may have problems with growth and development. There may be additional symptoms depending on the underlying cause. Iron-deficiency anemia is caused by blood loss, insufficient dietary intake, or Malabsorption, poor absorption of iron from food. Sources of blood loss can include heavy Menstruation, periods, childbirth, uterine fibroids, stomach ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemosiderin
Hemosiderin image of a kidney viewed under a microscope. The brown areas represent hemosiderin Hemosiderin or haemosiderin is an iron-storage complex that is composed of partially digested ferritin and lysosomes. The breakdown of heme gives rise to biliverdin and iron. The body then traps the released iron and stores it as hemosiderin in tissues. Hemosiderin is also generated from the abnormal metabolic pathway of ferritin. It is only found within cells (as opposed to circulating in blood) and appears to be a complex of ferritin, denatured ferritin and other material. The iron within deposits of hemosiderin is very poorly available to supply iron when needed. Hemosiderin can be identified histologically with '' Perls' Prussian blue stain''; iron in hemosiderin turns blue to black when exposed to potassium ferrocyanide. In normal animals, hemosiderin deposits are small and commonly inapparent without special stains. Excessive accumulation of hemosiderin is usually detected with ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iron
Iron is a chemical element; it has symbol Fe () and atomic number 26. It is a metal that belongs to the first transition series and group 8 of the periodic table. It is, by mass, the most common element on Earth, forming much of Earth's outer and inner core. It is the fourth most abundant element in the Earth's crust, being mainly deposited by meteorites in its metallic state. Extracting usable metal from iron ores requires kilns or furnaces capable of reaching , about 500 °C (900 °F) higher than that required to smelt copper. Humans started to master that process in Eurasia during the 2nd millennium BC and the use of iron tools and weapons began to displace copper alloys – in some regions, only around 1200 BC. That event is considered the transition from the Bronze Age to the Iron Age. In the modern world, iron alloys, such as steel, stainless steel, cast iron and special steels, are by far the most common industrial metals, due to their mechan ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iron Deficiency
Iron deficiency, or sideropenia, is the state in which a body lacks enough iron to supply its needs. Iron is present in all cells in the human body and has several vital functions, such as carrying oxygen to the tissues from the lungs as a key component of the hemoglobin protein, acting as a transport medium for electrons within the cells in the form of cytochromes, and facilitating oxygen enzyme reactions in various tissues. Too little iron can interfere with these vital functions and lead to morbidity and death. Total body iron averages approximately 3.8 g in men and 2.3 g in women. In blood plasma, iron is carried tightly bound to the protein transferrin. Several mechanisms control iron metabolism and safeguard against iron deficiency. The main regulatory mechanism is situated in the gastrointestinal tract. Most iron absorption occurs in the duodenum, the first section of the small intestine. Several dietary factors may affect iron absorption. Iron deficiency develops when ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biomineralization
Biomineralization, also written biomineralisation, is the process by which living organisms produce minerals, often resulting in hardened or stiffened '' mineralized tissues''. It is an extremely widespread phenomenon: all six taxonomic kingdoms contain members that can form minerals, and over 60 different minerals have been identified in organisms. Examples include silicates in algae and diatoms, carbonates in invertebrates, and calcium phosphates and carbonates in vertebrates. These minerals often form structural features such as sea shells and the bone in mammals and birds. Organisms have been producing mineralized skeletons for the past 550 million years. Calcium carbonates and calcium phosphates are usually crystalline, but silica organisms (such as sponges and diatoms) are always non-crystalline minerals. Other examples include copper, iron, and gold deposits involving bacteria. Biologically formed minerals often have special uses such as magnetic sensors in magnetota ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tyrosine
-Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a conditionally essential amino acid with a polar side group. The word "tyrosine" is from the Greek ''tyrós'', meaning ''cheese'', as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is encoded by the codons UAC and UAU in messenger RNA. The one-letter symbol Y was assigned to tyrosine for being alphabetically nearest of those letters available. Note that T was assigned to the structurally simpler threonine, U was avoided for its similarity with V for valine, W was assigned to tryptophan, while X was reserved for undetermined or atypical amino acids. The mnemonic t''Y''rosine was ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Untranslated Region
In molecular genetics, an untranslated region (or UTR) refers to either of two sections, one on each side of a coding sequence on a strand of mRNA. If it is found on the Directionality (molecular biology), 5' side, it is called the Five prime untranslated region, 5' UTR (or leader sequence), or if it is found on the Directionality (molecular biology), 3' side, it is called the Three prime untranslated region, 3' UTR (or trailer sequence). mRNA is RNA that carries information from DNA to the ribosome, the site of protein synthesis (Translation (biology), translation) within a cell. The mRNA is initially Transcription (genetics), transcribed from the corresponding DNA sequence and then translated into protein. However, several regions of the mRNA are usually not translated into protein, including the 5' and 3' UTRs. Although they are called untranslated regions, and do not form the Coding region, protein-coding region of the gene, Upstream open reading frame, uORFs located withi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Residue (chemistry)
In chemistry, residue is whatever remains or acts as a contaminant after a given class of events. Residue may be the material remaining after a process of preparation, separation, or purification, such as distillation, evaporation, or filtration. It may also denote the undesired by-products of a chemical reaction. Residues as an undesired by-product are a concern in agricultural and food industries. Food safety Toxic chemical residues, wastes or contamination from other processes, are a concern in food safety. The most common food residues originate from pesticides, veterinary drugs, and industrial chemicals. For example, the U.S. Food and Drug Administration (FDA) and the Canadian Food Inspection Agency (CFIA) have guidelines for detecting chemical residues that are possibly dangerous to consume. In the U.S., the FDA is responsible for setting guidelines while other organizations enforce them. Environmental concerns Similar to the food industry, in environmental science ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life. Amino acids can be classified according to the locations of the core structural functional groups ( alpha- , beta- , gamma- amino acids, etc.); other categories relate to polarity, ionization, and side-chain group type ( aliphatic, acyclic, aromatic, polar, etc.). In the form of proteins, amino-acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life on Earth and its emergence. Amino acids are formally named by the IUPAC- IUBMB Joint Commi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
